4-(9-diethylamino-5-oxo-5H-benzo[a]phenoxazin-3-yloxy)-butyric acid | 1018900-41-8

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并恶嗪类
• 英文名称: 4-(9-diethylamino-5-oxo-5H-benzo[a]phenoxazin-3-yloxy)-butyric acid
• 英文别名: 4-[9-(Diethylamino)-5-oxobenzo[a]phenoxazin-3-yl]oxybutanoic acid
• CAS: 1018900-41-8
• 化学式: C₂₄H₂₄N₂O₅
• 分子量: 420.465
• InChiKey: RSMWQUZHSQOILU-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.6
• 重原子数：
  31
• 可旋转键数：
  8
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  88.4
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  4-(9-diethylamino-5-oxo-5H-benzo[a]phenoxazin-3-yloxy)-butyric acid 2-trimethylsilanyl-ethyl ester 在 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 18.0h， 以95%的产率得到4-(9-diethylamino-5-oxo-5H-benzo[a]phenoxazin-3-yloxy)-butyric acid
  参考文献：
  名称：

  Probing lipid- and drug-binding domains with fluorescent dyes

  摘要：

  A series of 2- and 3-OH Nile red dyes was prepared in order to generate water-soluble probes that could be used to probe lipid binding to proteins. Various substitutions in positions 243-, 6-, and 7-shifted wavelengths while maintaining the environmental sensitivity of Nile red. In order to increase the solubility of the dyes in aqueous solutions, we attached butyric acid groups to the 2- or 3-OH position. In addition., phenothiazine dyes, which exhibited particularly long excitation properties, were synthesized and tested for the first time. All dyes showed Stoke's shifts of 70-100 nm and changes in excitation and emission of over 100 nm, depending on the hydrophobicity of the environment. Binding studies with bovine serum albumin and the non-specific lipid transfer protein SCP2 revealed emission changes of more than 30 nm upon binding to the protein and a five-fold increase in emission intensity. Titration of the dye-loaded proteins with various lipids or drugs replaced the dye and thereby reversed the shift in wavelength intensity. This allowed us to estimate the lipid binding affinity of the investigated proteins. For SCP2, isothermal calorimetry (ITC) data verified the titration experiments. NMR titration experiments of SCP2 with Nile red 2-O-butyric acid (1a) revealed that the dye is bound within the lipid binding pocket and competes with lipid ligands for this binding site. These results give valuable insight into lipid and drug transport by proteins outside and inside cells. (c) 2007 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2007.10.080

文献信息

• Probing lipid- and drug-binding domains with fluorescent dyes
  作者：Shannon L. Black、Will A. Stanley、Fabian V. Filipp、Michelle Bhairo、Ashwani Verma、Oliver Wichmann、Michael Sattler、Matthias Wilmanns、Carsten Schultz

  DOI：10.1016/j.bmc.2007.10.080

  日期：2008.2.1

  A series of 2- and 3-OH Nile red dyes was prepared in order to generate water-soluble probes that could be used to probe lipid binding to proteins. Various substitutions in positions 243-, 6-, and 7-shifted wavelengths while maintaining the environmental sensitivity of Nile red. In order to increase the solubility of the dyes in aqueous solutions, we attached butyric acid groups to the 2- or 3-OH position. In addition., phenothiazine dyes, which exhibited particularly long excitation properties, were synthesized and tested for the first time. All dyes showed Stoke's shifts of 70-100 nm and changes in excitation and emission of over 100 nm, depending on the hydrophobicity of the environment. Binding studies with bovine serum albumin and the non-specific lipid transfer protein SCP2 revealed emission changes of more than 30 nm upon binding to the protein and a five-fold increase in emission intensity. Titration of the dye-loaded proteins with various lipids or drugs replaced the dye and thereby reversed the shift in wavelength intensity. This allowed us to estimate the lipid binding affinity of the investigated proteins. For SCP2, isothermal calorimetry (ITC) data verified the titration experiments. NMR titration experiments of SCP2 with Nile red 2-O-butyric acid (1a) revealed that the dye is bound within the lipid binding pocket and competes with lipid ligands for this binding site. These results give valuable insight into lipid and drug transport by proteins outside and inside cells. (c) 2007 Elsevier Ltd. All rights reserved.